dbPTM

AN32A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AN32A_HUMAN
UniProt AC	P39687
Protein Name	Acidic leucine-rich nuclear phosphoprotein 32 family member A
Gene Name	ANP32A
Organism	Homo sapiens (Human).
Sequence Length	249
Subcellular Localization	Nucleus. Cytoplasm. Endoplasmic reticulum. Translocates to the cytoplasm during the process of neuritogenesis (By similarity). Shuttles between nucleus and cytoplasm..
Protein Description	Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1-mediated transcriptional repression..
Protein Sequence	MEMGRRIHLELRNRTPSDVKELVLDNSRSNEGKLEGLTDEFEELEFLSTINVGLTSIANLPKLNKLKKLELSDNRVSGGLEVLAEKCPNLTHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNDYRENVFKLLPQLTYLDGYDRDDKEAPDSDAEGYVEGLDDEEEDEDEEEYDEDAQVVEDEEDEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEELGEEERGQKRKREPEDEGEDDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Methylation	RRIHLELRNRTPSDV CCEEEECCCCCHHHH	22.62	-
15	Phosphorylation	HLELRNRTPSDVKEL EEECCCCCHHHHHHH	30.60	23927012
17	Phosphorylation	ELRNRTPSDVKELVL ECCCCCHHHHHHHHH	55.19	23927012
20	Ubiquitination	NRTPSDVKELVLDNS CCCHHHHHHHHHCCC	50.77	21890473
20	Acetylation	NRTPSDVKELVLDNS CCCHHHHHHHHHCCC	50.77	25953088
27	Phosphorylation	KELVLDNSRSNEGKL HHHHHCCCCCCCCCC	36.43	23401153
29	Phosphorylation	LVLDNSRSNEGKLEG HHHCCCCCCCCCCCC	38.77	25159151
68	Ubiquitination	PKLNKLKKLELSDNR CCCCCCCCCCCCCCC	58.59	-
75	Methylation	KLELSDNRVSGGLEV CCCCCCCCCCHHHHH	29.03	-
77	Phosphorylation	ELSDNRVSGGLEVLA CCCCCCCCHHHHHHH	24.73	21815630
86	Ubiquitination	GLEVLAEKCPNLTHL HHHHHHHHCCCCCEE	49.76	-
86	Acetylation	GLEVLAEKCPNLTHL HHHHHHHHCCCCCEE	49.76	25953088
87	S-nitrosylation	LEVLAEKCPNLTHLN HHHHHHHCCCCCEEE	1.71	2212679
96	Phosphorylation	NLTHLNLSGNKIKDL CCCEEECCCCCCCCH	38.97	72255823
99	Ubiquitination	HLNLSGNKIKDLSTI EEECCCCCCCCHHHC	55.44	21890473
99	Acetylation	HLNLSGNKIKDLSTI EEECCCCCCCCHHHC	55.44	25953088
101	Ubiquitination	NLSGNKIKDLSTIEP ECCCCCCCCHHHCHH	54.98	-
101	Acetylation	NLSGNKIKDLSTIEP ECCCCCCCCHHHCHH	54.98	19608861
104	Phosphorylation	GNKIKDLSTIEPLKK CCCCCCHHHCHHHHH	37.16	30266825
105	Phosphorylation	NKIKDLSTIEPLKKL CCCCCHHHCHHHHHH	36.34	28857561
110	Ubiquitination	LSTIEPLKKLENLKS HHHCHHHHHHHCCCC	67.06	21890473
110	Succinylation	LSTIEPLKKLENLKS HHHCHHHHHHHCCCC	67.06	23954790
110	Acetylation	LSTIEPLKKLENLKS HHHCHHHHHHHCCCC	67.06	23749302
116	Ubiquitination	LKKLENLKSLDLFNC HHHHHCCCCCCCCCC	61.63	-
117	Phosphorylation	KKLENLKSLDLFNCE HHHHCCCCCCCCCCE	30.22	20873877
123	Glutathionylation	KSLDLFNCEVTNLND CCCCCCCCEECCHHH	3.31	22555962
123	S-nitrosylation	KSLDLFNCEVTNLND CCCCCCCCEECCHHH	3.31	19483679
123	S-nitrosocysteine	KSLDLFNCEVTNLND CCCCCCCCEECCHHH	3.31	-
126	Phosphorylation	DLFNCEVTNLNDYRE CCCCCEECCHHHHHH	16.22	21406692
131	Phosphorylation	EVTNLNDYRENVFKL EECCHHHHHHHHHHH	20.82	21406692
132	Methylation	VTNLNDYRENVFKLL ECCHHHHHHHHHHHH	31.70	-
132	Dimethylation	VTNLNDYRENVFKLL ECCHHHHHHHHHHHH	31.70	-
137	Ubiquitination	DYRENVFKLLPQLTY HHHHHHHHHHHHHHC	44.85	-
143	Phosphorylation	FKLLPQLTYLDGYDR HHHHHHHHCCCCCCC	19.45	26356563
144	Phosphorylation	KLLPQLTYLDGYDRD HHHHHHHCCCCCCCC	16.04	26356563
148	Phosphorylation	QLTYLDGYDRDDKEA HHHCCCCCCCCCCCC	13.89	25884760
150	Methylation	TYLDGYDRDDKEAPD HCCCCCCCCCCCCCC	45.61	-
158	Phosphorylation	DDKEAPDSDAEGYVE CCCCCCCCCCCCCCC	37.35	26657352
163	Phosphorylation	PDSDAEGYVEGLDDE CCCCCCCCCCCCCCC	6.19	26074081
204	Phosphorylation	EGEEEDVSGEEEEDE CCCCCCCCCCHHHCC	53.46	15287743
238	Acetylation	EERGQKRKREPEDEG HHHHHHCCCCCCCCC	69.05	26051181
238	Methylation	EERGQKRKREPEDEG HHHHHHCCCCCCCCC	69.05	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
158	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
158	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
158	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
204	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
204	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
204	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AN32A_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of AN32A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAP1B_HUMAN	MAP1B	physical	12807913
XPO1_HUMAN	XPO1	physical	11565755
TAF1A_HUMAN	TAF1A	physical	11163245
SET_HUMAN	SET	physical	11163245
SET_HUMAN	SET	physical	17142970
H31_HUMAN	HIST1H3A	physical	15100215
IMA5_HUMAN	KPNA1	physical	16713569
IMA6_HUMAN	KPNA5	physical	16713569
IMA7_HUMAN	KPNA6	physical	16713569
PRGR_HUMAN	PGR	physical	15308690
THB_HUMAN	THRB	physical	15308690
PPARG_HUMAN	PPARG	physical	15308690
PCBP1_HUMAN	PCBP1	physical	21988832
ARC1B_HUMAN	ARPC1B	physical	22863883
IF4A3_HUMAN	EIF4A3	physical	22863883
PDLI5_HUMAN	PDLIM5	physical	22863883
RFA2_HUMAN	RPA2	physical	22863883
LA_HUMAN	SSB	physical	22863883
TPD54_HUMAN	TPD52L2	physical	22863883
PFD3_HUMAN	VBP1	physical	22863883
SAHH2_HUMAN	AHCYL1	physical	26344197
AN32B_HUMAN	ANP32B	physical	26344197
AN32E_HUMAN	ANP32E	physical	26344197
DMAP1_HUMAN	DMAP1	physical	26344197
PAPP1_HUMAN	PAPPA	physical	26344197
DCAF1_HUMAN	VPRBP	physical	26344197
VPS72_HUMAN	VPS72	physical	26344197
ELAV1_HUMAN	ELAVL1	physical	11565755

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AN32A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND MASSSPECTROMETRY.	17287340 [Abstract]